ID   PEPX_LACDA              Reviewed;         792 AA.
AC   Q1G9E8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Xaa-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE            EC=3.4.14.11 {ECO:0000255|HAMAP-Rule:MF_00698};
DE   AltName: Full=X-Pro dipeptidyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE   AltName: Full=X-prolyl-dipeptidyl aminopeptidase {ECO:0000255|HAMAP-Rule:MF_00698};
DE            Short=X-PDAP {ECO:0000255|HAMAP-Rule:MF_00698};
GN   Name=pepX {ECO:0000255|HAMAP-Rule:MF_00698}; OrderedLocusNames=Ldb1455;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS   / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS   00102 / Lb 14).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=390333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC   11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX   PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA   van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA   Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA   Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA   Weissenbach J., Ehrlich S.D., Maguin E.;
RT   "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT   and ongoing reductive evolution.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC   -!- FUNCTION: Removes N-terminal dipeptides sequentially from polypeptides
CC       having unsubstituted N-termini provided that the penultimate residue is
CC       proline. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes Xaa-Pro-|- bonds to release unblocked, N-terminal
CC         dipeptides from substrates including Ala-Pro-|-p-nitroanilide and
CC         (sequentially) Tyr-Pro-|-Phe-Pro-|-Gly-Pro-|-Ile.; EC=3.4.14.11;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00698};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00698}.
CC   -!- SIMILARITY: Belongs to the peptidase S15 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00698}.
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DR   EMBL; CR954253; CAI98255.1; -; Genomic_DNA.
DR   RefSeq; WP_011544058.1; NZ_JQAV01000009.1.
DR   AlphaFoldDB; Q1G9E8; -.
DR   SMR; Q1G9E8; -.
DR   STRING; 390333.Ldb1455; -.
DR   ESTHER; lacdl-pepx; Lactobacillus_peptidase.
DR   MEROPS; S15.001; -.
DR   EnsemblBacteria; CAI98255; CAI98255; Ldb1455.
DR   KEGG; ldb:Ldb1455; -.
DR   PATRIC; fig|390333.13.peg.1914; -.
DR   eggNOG; COG2936; Bacteria.
DR   HOGENOM; CLU_011800_0_0_9; -.
DR   OMA; LYTASPY; -.
DR   BioCyc; LDEL390333:LDB_RS06270-MON; -.
DR   Proteomes; UP000001259; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008239; F:dipeptidyl-peptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_00698; Aminopeptidase_S15; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR008252; Pept_S15_Xpro.
DR   InterPro; IPR015251; PepX_N_dom.
DR   InterPro; IPR036313; PepX_N_dom_sf.
DR   InterPro; IPR000383; Xaa-Pro-like_dom.
DR   InterPro; IPR013736; Xaa-Pro_dipept_C.
DR   Pfam; PF02129; Peptidase_S15; 1.
DR   Pfam; PF08530; PepX_C; 1.
DR   Pfam; PF09168; PepX_N; 1.
DR   PRINTS; PR00923; LACTOPTASE.
DR   SMART; SM00939; PepX_C; 1.
DR   SMART; SM00940; PepX_N; 1.
DR   SUPFAM; SSF49785; SSF49785; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   SUPFAM; SSF81761; SSF81761; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Serine protease.
FT   CHAIN           1..792
FT                   /note="Xaa-Pro dipeptidyl-peptidase"
FT                   /id="PRO_1000045480"
FT   ACT_SITE        363
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        482
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
FT   ACT_SITE        513
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00698"
SQ   SEQUENCE   792 AA;  88410 MW;  9078E795F2014F26 CRC64;
     MKYNQYAYVE TSPEKATEEL LAINFLPENY SSLSFSELLA VLTGNVLAEA TTRQAKDAKL
     AEFAVDDQTD LAAFLLDTPT AITASQFANV ALQLLGYHPN YDYSLTDPLT CGEKHALPAF
     KDLTSKEELI FAFYRLLNTR SKNGQILLDV MAGKGYFTQF WGEGKFMLFN GKSLPVFDTS
     QVIREVVYVQ SDLDTDGDGK GDLLPVTVFR PVESQDQLKV PALYTASPYF GGIIDNVKTN
     HNVDENLTDA TTWTNPKYVA KPLVKSPAPS GQDVPATELA TGQSSYGLNE YLLARGFASV
     FSGAIGNRHG DGIRITGSPE ETISQKEVIE WLTGDRVAYT DRTRRFETKA GWCSGNVGMT
     GRSYLGTLQI AIATTGVKGL KTVVSEAAIS SWYDYYREHG LVIAPSECQG EDMDKLAEVC
     QSNLWDGGNF TAKKAYEAEQ AELLAAQDRA TGQYSDFWES RNYRHHADGI KCSWISVHGL
     NDWNVKPKNV YKIWQKVKQL PVESHLFLHQ GPHYNMNNLV SIDFTDLMNL WFVHELLEVE
     NGAYEQWPKV MIQDNLEADK WHAESDWAND LGQASLYSPT ADGYLSTVEN GTGQLTFTDL
     GGTEFKKAGI SETDWEYQFI SGEKKWAKAS LRFESEEFLH PTTLVGRPKV QVRVAANKTV
     GQLSVALVDL GTRQRLTATP KIFARGNQPF GYRFEADSLQ EFVPDKATKA KLITKAHMNL
     QNYQDMKQPS KLEAGQFVDL EFELQPTYYT LPAGAKLCLI IYSTDQGMTK RPLETEDYTV
     DLAGTALLLY RK